K
Kari Alitalo
Researcher at University of Helsinki
Publications - 844
Citations - 122462
Kari Alitalo is an academic researcher from University of Helsinki. The author has contributed to research in topics: Angiogenesis & Vascular endothelial growth factor C. The author has an hindex of 174, co-authored 817 publications receiving 114231 citations. Previous affiliations of Kari Alitalo include Mount Sinai Hospital, Toronto & Cornell University.
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Patent
Modified vegf and pdgf with improved angiogenic properties
Kari Alitalo,Tuomas Tammela,Salla Keskitalo,Katri Pajusola,Markku M. Jeltsch,Seppo Ylä-Herttuala,Terhi Karpanen,Ulf Eriksson,Marko Uutela +8 more
TL;DR: In this paper, the authors present methods and compositions for making and using chimeric polypeptides that comprise a VEGFR-2 ligand, and the chimeric molecules of the present invention retain VEG FR-2 binding activity and an enhanced angiogenic activity as compared to native VEGF-A.
Journal ArticleDOI
Correction: EGFL7 loss correlates with increased VEGF-D expression, upregulating hippocampal adult neurogenesis and improving spatial learning and memory
Kathrin Barth,Verica Vasic,Brennan McDonald,Nora Heinig,Marc-Christoph Wagner,Ulrike Schumann,Cora Röhlecke,Frank Bicker,Lana Schumann,Konstantin Radyushkin,Jan Baumgart,Stefan Tenzer,Matthias Meinhardt,Kari Alitalo,Irmgard Tegeder,Mirko H. H. Schmidt +15 more
Posted ContentDOI
The blood vasculature instructs lymphatics patterning in a SOX7-dependent manner
Chiang Ikn,Winnie Luu,Jiang K,Kirschnick N,Mehdi Moustaqil,Davidson Tl,Emmanuelle Lesieur,Renae Skoczylas,Kouskoff,Kazenwadel J,Arriola-Martinez L,Emma Sierecki,Yann Gambin,Kari Alitalo,Friedemann Kiefer,Natasha L. Harvey,Mathias Francois +16 more
TL;DR: In this article, a BEC-specific transcription factor, SOX7, plays a crucial role in lymphatic vessel patterning by modulating the transcription of lymphangiocrine signals.
Patent
VEGF-C ΔR226ΔR227 mutants and uses thereof
Kari Alitalo,Vladimir Joukov +1 more
TL;DR: In this paper, the authors provided a list of VEGF-C polypeptides capable of binding to at least one of KDR receptor tyrosine kinase (VEGFR-2) and Flt4-RHTK-3.
Book ChapterDOI
A chimeric EGFR/neu receptor in studies of neu function.
TL;DR: Defining the role of neu in cellular transformation became a high-priority task in many laboratories around the world because of the intense interest in its cellular function.